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Conserved domains on  [gi|17538240|ref|NP_502120|]
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putative mitochondrial tRNA-specific 2-thiouridylase 1 [Caenorhabditis elegans]

Protein Classification

tRNA-specific 2-thiouridylase( domain architecture ID 10113449)

MnmA/TRMU family tRNA-specific 2-thiouridylase catalyzes the 2-thiolation of uridine at the wobble position of tRNAs

CATH:  2.30.30.280|3.40.50.620
EC:  2.8.1.-
Gene Ontology:  GO:0005524|GO:0000049|GO:0006400|GO:0016783
PubMed:  16387657|16871210|12012333
SCOP:  4007171

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
 3-368 1.06e-157

MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


:

Pssm-ID: 467502 [Multi-domain]  Cd Length: 349  Bit Score: 446.57  E-value: 1.06e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240   3 RVVIGMSGGVDSAVSAFLLKKRGFDVIGLHMINWDVQEEGTSHCPRSKDESDARNVCDRLNIPFHTVNFVKEYWNDVFLK 82
Cdd:cd01998   1 KVAVAMSGGVDSSVAAALLKEQGYDVIGVFMKNWDDEDNEKGGCCSEEDIEDARRVADQLGIPLYVVDFSEEYWERVFDP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240  83 FLENYKNGRTTVPDIDCNQSIKFDVFHKIAReKFNADFIATGHYATTNFGdfqqnakDSDEIRLFSGKDPLKDQTFFLCT 162
Cdd:cd01998  81 FLEEYKAGRTPNPDVLCNREIKFGALLDAAK-KLGADYIATGHYARIEED-------NRGRYRLLRAVDPNKDQSYFLSR 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240 163 VNQEQLKRAMFPLGSLQKSEVKRIAEEQGFqEVAKKPESMGICFIGKKKrFSDFLDEYIEPK-PGRILLKNGSEIGNHHG 241
Cdd:cd01998 153 LSQEQLSRTLFPLGHLTKSEVREIAREAGL-PVAEKKDSQGICFIGKRD-FRDFLKEYLPEKlPGPIVDIDGKVLGEHKG 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240 242 IHQFTIGKR--INGKYLEARshlgfFVSHIHSDTGDIIACEGshHPDLYASRFLINHPKWIRTFDPFNrisSNNFLCRIQ 319
Cdd:cd01998 231 LWFYTIGQRkgLGIAAGEPL-----YVVKKDPEKNIVVVGPG--HPALFSDTLRASDLNWISPEPPLE---PLECEAKIR 300

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 17538240 320 RTHPPIPCVAEKQEQ-FLSVIPRLALRATAPGQMCVFYNtKNECLGGGEI 368
Cdd:cd01998 301 YRQPPVPCTVTPLDDgRLKVEFDEPQRAVTPGQAAVFYD-GDEVLGGGII 349
 
Name Accession Description Interval E-value
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
 3-368 1.06e-157

MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467502 [Multi-domain]  Cd Length: 349  Bit Score: 446.57  E-value: 1.06e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240   3 RVVIGMSGGVDSAVSAFLLKKRGFDVIGLHMINWDVQEEGTSHCPRSKDESDARNVCDRLNIPFHTVNFVKEYWNDVFLK 82
Cdd:cd01998   1 KVAVAMSGGVDSSVAAALLKEQGYDVIGVFMKNWDDEDNEKGGCCSEEDIEDARRVADQLGIPLYVVDFSEEYWERVFDP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240  83 FLENYKNGRTTVPDIDCNQSIKFDVFHKIAReKFNADFIATGHYATTNFGdfqqnakDSDEIRLFSGKDPLKDQTFFLCT 162
Cdd:cd01998  81 FLEEYKAGRTPNPDVLCNREIKFGALLDAAK-KLGADYIATGHYARIEED-------NRGRYRLLRAVDPNKDQSYFLSR 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240 163 VNQEQLKRAMFPLGSLQKSEVKRIAEEQGFqEVAKKPESMGICFIGKKKrFSDFLDEYIEPK-PGRILLKNGSEIGNHHG 241
Cdd:cd01998 153 LSQEQLSRTLFPLGHLTKSEVREIAREAGL-PVAEKKDSQGICFIGKRD-FRDFLKEYLPEKlPGPIVDIDGKVLGEHKG 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240 242 IHQFTIGKR--INGKYLEARshlgfFVSHIHSDTGDIIACEGshHPDLYASRFLINHPKWIRTFDPFNrisSNNFLCRIQ 319
Cdd:cd01998 231 LWFYTIGQRkgLGIAAGEPL-----YVVKKDPEKNIVVVGPG--HPALFSDTLRASDLNWISPEPPLE---PLECEAKIR 300

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 17538240 320 RTHPPIPCVAEKQEQ-FLSVIPRLALRATAPGQMCVFYNtKNECLGGGEI 368
Cdd:cd01998 301 YRQPPVPCTVTPLDDgRLKVEFDEPQRAVTPGQAAVFYD-GDEVLGGGII 349
MnmA COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
 3-368 4.08e-138

tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]; tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440250 [Multi-domain]  Cd Length: 353  Bit Score: 397.12  E-value: 4.08e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240   3 RVVIGMSGGVDSAVSAFLLKKRGFDVIGLHMINWD-VQEEGTSHCPRSKDESDARNVCDRLNIPFHTVNFVKEYWNDVFL 81
Cdd:COG0482   2 RVVVGMSGGVDSSVAAALLKEQGYEVIGVTMKLWDdDDASGSGGCCSLEDIEDARRVADKLGIPHYVVDFEEEFKDRVID 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240  82 KFLENYKNGRTTVPDIDCNQSIKFDVFHKIAREkFNADFIATGHYAttnfgdfqQNAKDSDEIRLFSGKDPLKDQTFFLC 161
Cdd:COG0482  82 YFLDEYLAGRTPNPCVLCNREIKFGALLEKALE-LGADYIATGHYA--------RVEEKDGRYELLRGVDPNKDQSYFLY 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240 162 TVNQEQLKRAMFPLGSLQKSEVKRIAEEQGFqEVAKKPESMGICFIGkKKRFSDFLDEYIEPKPGRILLKNGSEIGNHHG 241
Cdd:COG0482 153 RLTQEQLSKTLFPLGELTKPEVREIAEELGL-PVADKKDSQGICFIG-DGDYRDFLERYLPEKPGDIVDLDGKVLGEHDG 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240 242 IHQFTIGKR----INGKylEARshlgfFVSHIHSDTGDIIACEGShhpDLYASRFLINHPKWIRTFDPfnrisSNNFLCR 317
Cdd:COG0482 231 LHYYTIGQRkglgIGGG--EPL-----YVVGKDPETNTVIVGQGE---ALYSRELTAEDVNWISGEPP-----EEPLRCT 295

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 17538240 318 IQ-R-THPPIPCVAEKQE-QFLSVIPRLALRATAPGQMCVFYNtKNECLGGGEI 368
Cdd:COG0482 296 AKiRyRQPPVPATLTPLEdGRVRVEFDEPQRAVTPGQSAVFYD-GDRVLGGGII 348
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
 3-368 1.19e-137

tRNA-specific 2-thiouridylase MnmA; Reviewed


Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 395.59  E-value: 1.19e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240    3 RVVIGMSGGVDSAVSAFLLKKRGFDVIGLHMINWD-VQEEGTSHCPRSKDESDARNVCDRLNIPFHTVNFVKEYWNDVFL 81
Cdd:PRK00143   2 RVVVGMSGGVDSSVAAALLKEQGYEVIGVFMKLWDdDDETGKGGCCAEEDIADARRVADKLGIPHYVVDFEKEFWDRVID 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240   82 KFLENYKNGRTTVPDIDCNQSIKFDVFHKIAREkFNADFIATGHYATTNFGdfqqnakdsdeIRLFSGKDPLKDQTFFLC 161
Cdd:PRK00143  82 YFLDEYKAGRTPNPCVLCNKEIKFKAFLEYARE-LGADYIATGHYARIRDG-----------RELLRGVDPNKDQSYFLY 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240  162 TVNQEQLKRAMFPLGSLQKSEVKRIAEEQGFqEVAKKPESMGICFIGKKKrFSDFLDEYIEPKPGRILLKNGSEIGNHHG 241
Cdd:PRK00143 150 QLTQEQLAKLLFPLGELTKPEVREIAEEAGL-PVAKKKDSQGICFIGERD-YRDFLKRYLPAQPGEIVDLDGKVLGEHKG 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240  242 IHQFTIGKRingKYLE-ARSHLGFFVSHIHSDTGDIIAcegSHHPDLYASRFLINHPKWIRTFDPFNRIssnNFLCRIQR 320
Cdd:PRK00143 228 LMYYTIGQR---KGLGiGGDGEPWYVVGKDPETNTVVV---GQGEALYSRELIASDLNWVGGEPPEEPF---ECTAKIRY 298

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 17538240  321 THPPIPCVAEKQEQFLSVIPRLALRATAPGQMCVFYNtKNECLGGGEI 368
Cdd:PRK00143 299 RQKPVPATVELEDDRVEVEFDEPQRAVTPGQAAVFYD-GDRVLGGGII 345
trmU TIGR00420
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ...
 3-368 2.06e-109

tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase (trmU, asuE, or mnmA) is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine (mnm5s2U34) present in the wobble position of some tRNAs. This enzyme appears not to occur in the Archaea. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273069 [Multi-domain]  Cd Length: 352  Bit Score: 324.34  E-value: 2.06e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240     3 RVVIGMSGGVDSAVSAFLLKKRGFDVIGLHMINWDVQEEGTSH-CPRSKDESDARNVCDRLNIPFHTVNFVKEYWNDVFL 81
Cdd:TIGR00420   2 KVIVGLSGGVDSSVSAYLLKQQGYEVVGVFMKNWEEDDKNDGHgCTSAEDLRDAQAICEKLGIPLEKVNFQKEYWNKVFE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240    82 KFLENYKNGRTTVPDIDCNQSIKFDVFHKIAREKFNADFIATGHYATTNFGDFQQnakdsdeiRLFSGKDPLKDQTFFLC 161
Cdd:TIGR00420  82 PFIQEYKEGRTPNPDILCNKFIKFGAFLEYAAELLGNDKIATGHYARIAEIEGKS--------LLLRALDKNKDQSYFLY 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240   162 TVNQEQLKRAMFPLGSLQKSEVKRIAEEQGFqEVAKKPESMGICFIGKKKrFSDFLDEYIEPKPGRIL-LKNGSEIGNHH 240
Cdd:TIGR00420 154 HLSHEQLAKLLFPLGELLKPEVRQIAKNAGL-PTAEKKDSQGICFIGERK-FRDFLKKYLPVKPGVIItVDGQSVIGEHD 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240   241 GIHQFTIGKR--IN-GKYLEArshlgFFVSHIHSDTGDIIAceGSHHPDLYASRFLINHPKWI-RTFDPFnrisSNNFLC 316
Cdd:TIGR00420 232 GLWFYTIGQRkgLGiGGAAEP-----WFVVEKDLETNELVV--SHGKPDLASRGLLAQQFHWLdDEPNPF----EMRCTV 300

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 17538240   317 RIQRTHPPIPCVAEKQ-EQFLSVIPRLALRATAPGQMCVFYnTKNECLGGGEI 368
Cdd:TIGR00420 301 KIRYRQVPVQCKLKLLdDNLIEVIFDEPQAGVTPGQSAVLY-KGDICLGGGII 352
tRNA_Me_trans pfam03054
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ...
 3-209 1.14e-94

tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.


Pssm-ID: 460787 [Multi-domain]  Cd Length: 202  Bit Score: 281.06  E-value: 1.14e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240     3 RVVIGMSGGVDSAVSAFLLKKRGFDVIGLHMINWDVQ--EEGTSHCPRSKDESDARNVCDRLNIPFHTVNFVKEYWNDVF 80
Cdd:pfam03054   2 KVVVAMSGGVDSSVAAYLLKEQGHNVIGVFMKNWDEEqsLDEEGKCCSEEDLADAQRVCEQLGIPLYVVNFEKEYWEDVF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240    81 LKFLENYKNGRTTVPDIDCNQSIKFDVFHKIAREKFNADFIATGHYATTNFGdfqqnakDSDEIRLFSGKDPLKDQTFFL 160
Cdd:pfam03054  82 EPFLDEYKNGRTPNPDVLCNKEIKFGALLDYALENLGADYVATGHYARVSLN-------KDGGSELLRALDKNKDQSYFL 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 17538240   161 CTVNQEQLKRAMFPLGSLQKSEVKRIAEEQGFQeVAKKPESMGICFIGK 209
Cdd:pfam03054 155 STLSQEQLEKLLFPLGELTKEEVRKIAKEAGLA-TAKKKDSQGICFIGK 202
 
Name Accession Description Interval E-value
MnmA_TRMU-like cd01998
MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial ...
 3-368 1.06e-157

MnmA/TRMU family 2-thiouridylases and similar proteins; This family is composed of bacterial tRNA-specific 2-thiouridylase MnmA (EC 2.8.1.13) and mitochondrial tRNA-specific 2-thiouridylase 1 (TRMU or MTU1, EC 2.8.1.14). MnmA catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34. TRMU/MTU1 catalyzes the 2-thiolation of uridine at the wobble position (U34) of mitochondrial tRNA(Lys), tRNA(Glu) and tRNA(Gln); this is required for the formation of 5-taurinomethyl-2-thiouridine (tm5s2U) of mitochondrial tRNA(Lys), tRNA(Glu), and tRNA(Gln) at the wobble position. This family belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467502 [Multi-domain]  Cd Length: 349  Bit Score: 446.57  E-value: 1.06e-157
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240   3 RVVIGMSGGVDSAVSAFLLKKRGFDVIGLHMINWDVQEEGTSHCPRSKDESDARNVCDRLNIPFHTVNFVKEYWNDVFLK 82
Cdd:cd01998   1 KVAVAMSGGVDSSVAAALLKEQGYDVIGVFMKNWDDEDNEKGGCCSEEDIEDARRVADQLGIPLYVVDFSEEYWERVFDP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240  83 FLENYKNGRTTVPDIDCNQSIKFDVFHKIAReKFNADFIATGHYATTNFGdfqqnakDSDEIRLFSGKDPLKDQTFFLCT 162
Cdd:cd01998  81 FLEEYKAGRTPNPDVLCNREIKFGALLDAAK-KLGADYIATGHYARIEED-------NRGRYRLLRAVDPNKDQSYFLSR 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240 163 VNQEQLKRAMFPLGSLQKSEVKRIAEEQGFqEVAKKPESMGICFIGKKKrFSDFLDEYIEPK-PGRILLKNGSEIGNHHG 241
Cdd:cd01998 153 LSQEQLSRTLFPLGHLTKSEVREIAREAGL-PVAEKKDSQGICFIGKRD-FRDFLKEYLPEKlPGPIVDIDGKVLGEHKG 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240 242 IHQFTIGKR--INGKYLEARshlgfFVSHIHSDTGDIIACEGshHPDLYASRFLINHPKWIRTFDPFNrisSNNFLCRIQ 319
Cdd:cd01998 231 LWFYTIGQRkgLGIAAGEPL-----YVVKKDPEKNIVVVGPG--HPALFSDTLRASDLNWISPEPPLE---PLECEAKIR 300

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 17538240 320 RTHPPIPCVAEKQEQ-FLSVIPRLALRATAPGQMCVFYNtKNECLGGGEI 368
Cdd:cd01998 301 YRQPPVPCTVTPLDDgRLKVEFDEPQRAVTPGQAAVFYD-GDEVLGGGII 349
MnmA COG0482
tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ...
 3-368 4.08e-138

tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain [Translation, ribosomal structure and biogenesis]; tRNA U34 2-thiouridine synthase MnmA/TrmU, contains the PP-loop ATPase domain is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440250 [Multi-domain]  Cd Length: 353  Bit Score: 397.12  E-value: 4.08e-138
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240   3 RVVIGMSGGVDSAVSAFLLKKRGFDVIGLHMINWD-VQEEGTSHCPRSKDESDARNVCDRLNIPFHTVNFVKEYWNDVFL 81
Cdd:COG0482   2 RVVVGMSGGVDSSVAAALLKEQGYEVIGVTMKLWDdDDASGSGGCCSLEDIEDARRVADKLGIPHYVVDFEEEFKDRVID 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240  82 KFLENYKNGRTTVPDIDCNQSIKFDVFHKIAREkFNADFIATGHYAttnfgdfqQNAKDSDEIRLFSGKDPLKDQTFFLC 161
Cdd:COG0482  82 YFLDEYLAGRTPNPCVLCNREIKFGALLEKALE-LGADYIATGHYA--------RVEEKDGRYELLRGVDPNKDQSYFLY 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240 162 TVNQEQLKRAMFPLGSLQKSEVKRIAEEQGFqEVAKKPESMGICFIGkKKRFSDFLDEYIEPKPGRILLKNGSEIGNHHG 241
Cdd:COG0482 153 RLTQEQLSKTLFPLGELTKPEVREIAEELGL-PVADKKDSQGICFIG-DGDYRDFLERYLPEKPGDIVDLDGKVLGEHDG 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240 242 IHQFTIGKR----INGKylEARshlgfFVSHIHSDTGDIIACEGShhpDLYASRFLINHPKWIRTFDPfnrisSNNFLCR 317
Cdd:COG0482 231 LHYYTIGQRkglgIGGG--EPL-----YVVGKDPETNTVIVGQGE---ALYSRELTAEDVNWISGEPP-----EEPLRCT 295

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 17538240 318 IQ-R-THPPIPCVAEKQE-QFLSVIPRLALRATAPGQMCVFYNtKNECLGGGEI 368
Cdd:COG0482 296 AKiRyRQPPVPATLTPLEdGRVRVEFDEPQRAVTPGQSAVFYD-GDRVLGGGII 348
mnmA PRK00143
tRNA-specific 2-thiouridylase MnmA; Reviewed
 3-368 1.19e-137

tRNA-specific 2-thiouridylase MnmA; Reviewed


Pssm-ID: 234664 [Multi-domain]  Cd Length: 346  Bit Score: 395.59  E-value: 1.19e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240    3 RVVIGMSGGVDSAVSAFLLKKRGFDVIGLHMINWD-VQEEGTSHCPRSKDESDARNVCDRLNIPFHTVNFVKEYWNDVFL 81
Cdd:PRK00143   2 RVVVGMSGGVDSSVAAALLKEQGYEVIGVFMKLWDdDDETGKGGCCAEEDIADARRVADKLGIPHYVVDFEKEFWDRVID 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240   82 KFLENYKNGRTTVPDIDCNQSIKFDVFHKIAREkFNADFIATGHYATTNFGdfqqnakdsdeIRLFSGKDPLKDQTFFLC 161
Cdd:PRK00143  82 YFLDEYKAGRTPNPCVLCNKEIKFKAFLEYARE-LGADYIATGHYARIRDG-----------RELLRGVDPNKDQSYFLY 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240  162 TVNQEQLKRAMFPLGSLQKSEVKRIAEEQGFqEVAKKPESMGICFIGKKKrFSDFLDEYIEPKPGRILLKNGSEIGNHHG 241
Cdd:PRK00143 150 QLTQEQLAKLLFPLGELTKPEVREIAEEAGL-PVAKKKDSQGICFIGERD-YRDFLKRYLPAQPGEIVDLDGKVLGEHKG 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240  242 IHQFTIGKRingKYLE-ARSHLGFFVSHIHSDTGDIIAcegSHHPDLYASRFLINHPKWIRTFDPFNRIssnNFLCRIQR 320
Cdd:PRK00143 228 LMYYTIGQR---KGLGiGGDGEPWYVVGKDPETNTVVV---GQGEALYSRELIASDLNWVGGEPPEEPF---ECTAKIRY 298

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 17538240  321 THPPIPCVAEKQEQFLSVIPRLALRATAPGQMCVFYNtKNECLGGGEI 368
Cdd:PRK00143 299 RQKPVPATVELEDDRVEVEFDEPQRAVTPGQAAVFYD-GDRVLGGGII 345
trmU TIGR00420
tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA ...
 3-368 2.06e-109

tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase; tRNA (5-methylaminomethyl-2-thiouridylate)-methyltransferase (trmU, asuE, or mnmA) is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine (mnm5s2U34) present in the wobble position of some tRNAs. This enzyme appears not to occur in the Archaea. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273069 [Multi-domain]  Cd Length: 352  Bit Score: 324.34  E-value: 2.06e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240     3 RVVIGMSGGVDSAVSAFLLKKRGFDVIGLHMINWDVQEEGTSH-CPRSKDESDARNVCDRLNIPFHTVNFVKEYWNDVFL 81
Cdd:TIGR00420   2 KVIVGLSGGVDSSVSAYLLKQQGYEVVGVFMKNWEEDDKNDGHgCTSAEDLRDAQAICEKLGIPLEKVNFQKEYWNKVFE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240    82 KFLENYKNGRTTVPDIDCNQSIKFDVFHKIAREKFNADFIATGHYATTNFGDFQQnakdsdeiRLFSGKDPLKDQTFFLC 161
Cdd:TIGR00420  82 PFIQEYKEGRTPNPDILCNKFIKFGAFLEYAAELLGNDKIATGHYARIAEIEGKS--------LLLRALDKNKDQSYFLY 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240   162 TVNQEQLKRAMFPLGSLQKSEVKRIAEEQGFqEVAKKPESMGICFIGKKKrFSDFLDEYIEPKPGRIL-LKNGSEIGNHH 240
Cdd:TIGR00420 154 HLSHEQLAKLLFPLGELLKPEVRQIAKNAGL-PTAEKKDSQGICFIGERK-FRDFLKKYLPVKPGVIItVDGQSVIGEHD 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240   241 GIHQFTIGKR--IN-GKYLEArshlgFFVSHIHSDTGDIIAceGSHHPDLYASRFLINHPKWI-RTFDPFnrisSNNFLC 316
Cdd:TIGR00420 232 GLWFYTIGQRkgLGiGGAAEP-----WFVVEKDLETNELVV--SHGKPDLASRGLLAQQFHWLdDEPNPF----EMRCTV 300

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 17538240   317 RIQRTHPPIPCVAEKQ-EQFLSVIPRLALRATAPGQMCVFYnTKNECLGGGEI 368
Cdd:TIGR00420 301 KIRYRQVPVQCKLKLLdDNLIEVIFDEPQAGVTPGQSAVLY-KGDICLGGGII 352
tRNA_Me_trans pfam03054
tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA ...
 3-209 1.14e-94

tRNA methyl transferase HUP domain; This family represents the N-terminal HUP domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.


Pssm-ID: 460787 [Multi-domain]  Cd Length: 202  Bit Score: 281.06  E-value: 1.14e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240     3 RVVIGMSGGVDSAVSAFLLKKRGFDVIGLHMINWDVQ--EEGTSHCPRSKDESDARNVCDRLNIPFHTVNFVKEYWNDVF 80
Cdd:pfam03054   2 KVVVAMSGGVDSSVAAYLLKEQGHNVIGVFMKNWDEEqsLDEEGKCCSEEDLADAQRVCEQLGIPLYVVNFEKEYWEDVF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240    81 LKFLENYKNGRTTVPDIDCNQSIKFDVFHKIAREKFNADFIATGHYATTNFGdfqqnakDSDEIRLFSGKDPLKDQTFFL 160
Cdd:pfam03054  82 EPFLDEYKNGRTPNPDVLCNKEIKFGALLDYALENLGADYVATGHYARVSLN-------KDGGSELLRALDKNKDQSYFL 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 17538240   161 CTVNQEQLKRAMFPLGSLQKSEVKRIAEEQGFQeVAKKPESMGICFIGK 209
Cdd:pfam03054 155 STLSQEQLEKLLFPLGELTKEEVRKIAKEAGLA-TAKKKDSQGICFIGK 202
PRK14664 PRK14664
tRNA-specific 2-thiouridylase MnmA; Provisional
 3-368 3.75e-51

tRNA-specific 2-thiouridylase MnmA; Provisional


Pssm-ID: 173127 [Multi-domain]  Cd Length: 362  Bit Score: 174.76  E-value: 3.75e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240    3 RVVIGMSGGVDSAVSAFLLKKRGFDVIGLHMINWDvqeegtshcprskDE-SDARNVCDRLNIPFHTVNFVKEYWNDVFL 81
Cdd:PRK14664   7 RVLVGMSGGIDSTATCLMLQEQGYEIVGVTMRVWG-------------DEpQDARELAARMGIEHYVADERVPFKDTIVK 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240   82 KFLENYKNGRTTVPDIDCNQSIKFDVFHKIArEKFNADFIATGHYATTNfgdfqqnaKDSDEIRLFSGKDPLKDQTFFLC 161
Cdd:PRK14664  74 NFIDEYRQGRTPNPCVMCNPLFKFRMLIEWA-DKLGCAWIATGHYSRLE--------ERNGHIYIVAGDDDKKDQSYFLW 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240  162 TVNQEQLKRAMFPLGSLQKSEVKRIAEEQGFQEVAKKPESMGICFIgkKKRFSDFLDEY-----IEPKPGRILLKNGSEI 236
Cdd:PRK14664 145 RLGQDILRRCIFPLGNYTKQTVREYLREKGYEAKSKEGESMEVCFI--KGDYRDFLREQcpeldTEVGPGWFVNSEGVKL 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240  237 GNHHGIHQFTIGKRingKYLEARSHLGFFVSHIHSDTGDIIACEGShhpDLYASRFLINHPKWIRTFDPFnriSSNNFLC 316
Cdd:PRK14664 223 GQHKGFPYYTIGQR---KGLEIALGKPAYVLKINPQKNTVMLGDAE---QLKAEYMLAEQDNIVDEQELF---ACPDLAV 293

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 17538240  317 RIQRTHPPIPC-VAEKQEQFLSVIPRLALRATAPGQMCVFYNTKnECLGGGEI 368
Cdd:PRK14664 294 RIRYRSRPIPCrVKRLEDGRLLVRFLAEASAIAPGQSAVFYEGR-RVLGGAFI 345
mnmA PRK14665
tRNA-specific 2-thiouridylase MnmA; Provisional
 3-369 2.70e-46

tRNA-specific 2-thiouridylase MnmA; Provisional


Pssm-ID: 173128 [Multi-domain]  Cd Length: 360  Bit Score: 162.02  E-value: 2.70e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240    3 RVVIGMSGGVDSAVSAFLLKKRGFDVIGLHMINWDVqEEGTSHCprskdeSDARNVCDRLNIPFHTVNFVKEYWNDVFLK 82
Cdd:PRK14665   7 RVLLGMSGGTDSSVAAMLLLEAGYEVTGVTFRFYEF-NGSTEYL------EDARALAERLGIGHITYDARKVFRKQIIDY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240   83 FLENYKNGRTTVPDIDCNQSIKFDVFHKIAREkFNADFIATGHYATTNFGDfqqnakdsDEIRLFSGKDPLKDQTFFLCT 162
Cdd:PRK14665  80 FIDEYMSGHTPVPCTLCNNYLKWPLLAKIADE-MGIFYLATGHYVRKQWID--------GNYYITPAEDVDKDQSFFLWG 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240  163 VNQEQLKRAMFPLGSLQKSEVKRIAEEQGFQEVAKKPESMGICFIGKKKRfsDFLDE-------------YIEPKPGRIL 229
Cdd:PRK14665 151 LRQEILQRMLLPMGGMTKSEARAYAAERGFEKVAKKRDSLGVCFCPMDYR--SFLKKclcdesgdknrniYRKVERGRFL 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240  230 LKNGSEIGNHHGIHQFTIGKRingKYLEARSHLGFFVSHIHSDTGDIIacegshhpdLYASRFLINHPKWIRTFDPFNR- 308
Cdd:PRK14665 229 DESGNFIAWHEGYPFYTIGQR---RGLGIQLNRAVFVKEIHPETNEVV---------LASLKALEKTEMWLKDWNIVNEs 296

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17538240  309 --ISSNNFLCRIQRTHPPIPC-VAEKQEQFLSVIPRLALRATAPGQMCVFYNtKNECLGGGEIM 369
Cdd:PRK14665 297 rlLGCDDIIVKIRYRKQENHCtVTITPDNLLHVQLHEPLTAIAEGQAAAFYK-DGLLLGGGIIT 359
lysidine_TilS_N TIGR02432
tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble ...
 3-191 1.53e-10

tRNA(Ile)-lysidine synthetase, N-terminal domain; The only examples in which the wobble position of a tRNA must discriminate between G and A of mRNA are AUA (Ile) vs. AUG (Met) and UGA (stop) vs. UGG (Trp). In all bacteria, the wobble position of the tRNA(Ile) recognizing AUA is lysidine, a lysine derivative of cytidine. This family describes a protein domain found, apparently, in all bacteria in a single copy. Eukaryotic sequences appear to be organellar. The domain archictecture of this protein family is variable; some, including characterized proteins of E. coli and B. subtilis known to be tRNA(Ile)-lysidine synthetase, include a conserved 50-residue domain that many other members lack. This protein belongs to the ATP-binding PP-loop family ( pfam01171). It appears in the literature and protein databases as TilS, YacA, and putative cell cycle protein MesJ (a misnomer). [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274129 [Multi-domain]  Cd Length: 189  Bit Score: 59.95  E-value: 1.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240     3 RVVIGMSGGVDSAVSAFLLKKR----GFDVIGLHmINwdvqeegtsHCPRSKDESDARNV---CDRLNIPFHTVNF-VKE 74
Cdd:TIGR02432   1 RILVAVSGGVDSMALLHLLLKLqpkiKIKLIAAH-VD---------HGLRPESDEEAEFVqqfCRKLNIPLEIKKVdVKA 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240    75 YWNDVFLKFLENYKNGRttvpdidcnqsikFDVFHKIArEKFNADFIATGHyattnfgdfqqNAKDSDE---IRLFSGKD 151
Cdd:TIGR02432  71 LAKGKKKNLEEAAREAR-------------YDFFEEIA-KKHGADYILTAH-----------HADDQAEtilMRLLRGSG 125

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 17538240   152 P-----LKDQTFFlctVNQEQLKRamfPLGSLQKSEVKRIAEEQG 191
Cdd:TIGR02432 126 LrglsgMKPIRIL---GSGIQIIR---PLLGISKSEIEEYLKENG 164
TilS COG0037
tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA ...
 3-125 5.47e-10

tRNA(Ile)-lysidine synthase TilS/MesJ [Translation, ribosomal structure and biogenesis]; tRNA(Ile)-lysidine synthase TilS/MesJ is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439807 [Multi-domain]  Cd Length: 235  Bit Score: 59.08  E-value: 5.47e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240   3 RVVIGMSGGVDSAVSAFLLKK----RGFDVIGLHmINWDVQEEgtshcpRSKDESDARNVCDRLNIPFHTVNF-VKEYWN 77
Cdd:COG0037  17 RILVAVSGGKDSLALLHLLAKlrrrLGFELVAVH-VDHGLREE------SDEDAEFVAELCEELGIPLHVVRVdVPAIAK 89

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 17538240  78 dvflkflenyKNGRTTvpdidcnQS----IKFDVFHKIAREKfNADFIATGH 125
Cdd:COG0037  90 ----------KEGKSP-------EAaarrARYGALYELAREL-GADKIATGH 123
PRK13980 PRK13980
NAD synthetase; Provisional
 3-70 4.09e-09

NAD synthetase; Provisional


Pssm-ID: 184435 [Multi-domain]  Cd Length: 265  Bit Score: 56.76  E-value: 4.09e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240    3 RVVIGMSGGVDSAVSAFLLKKR-GFD-VIGLHMinwdvqeegTSHCPRSKDESDARNVCDRLNIPFHTVN 70
Cdd:PRK13980  32 GVVLGLSGGIDSAVVAYLAVKAlGKEnVLALLM---------PSSVSPPEDLEDAELVAEDLGIEYKVIE 92
tRNA_Me_trans_M pfam20259
tRNA methyl transferase PRC-barrel domain; This family represents a central PRC-barrel domain ...
 214-280 5.45e-09

tRNA methyl transferase PRC-barrel domain; This family represents a central PRC-barrel domain in tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.


Pssm-ID: 466410 [Multi-domain]  Cd Length: 66  Bit Score: 52.22  E-value: 5.45e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17538240   214 SDFLDEYIEPKPGRIL-LKNGSEIGNHHGIHQFTIGKRIN---GKYLEARshlgfFVSHIHSDTGDIIACE 280
Cdd:pfam20259   1 KDFLKEYLPVKPGDIIdIDTGEVLGEHEGIWFYTIGQRKGlgiGGYGEPW-----YVVEKDPKKNTVYVGR 66
tRNA_Me_trans_C pfam20258
Aminomethyltransferase beta-barrel domain; This domain is found at the C-terminus of tRNA ...
 292-368 6.99e-09

Aminomethyltransferase beta-barrel domain; This domain is found at the C-terminus of tRNA(5-methylaminomethyl-2-thiouridine)-methyltransferase which is involved in the biosynthesis of the modified nucleoside 5-methylaminomethyl-2-thiouridine present in the wobble position of some tRNAs.


Pssm-ID: 466409 [Multi-domain]  Cd Length: 77  Bit Score: 52.28  E-value: 6.99e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17538240   292 FLINHPKWIRTFDPFNRISsnnFLCRIQRTHPPIPCVAEKQE-QFLSVIPRLALRATAPGQMCVFY-NTknECLGGGEI 368
Cdd:pfam20258   4 LRAKDPNWLGDKPPTEPLE---CTVKVRHRQPPVPCVVELIDdETVEVHFDEPVRAVTPGQAAVFYdGD--RCLGGGII 77
NadE COG0171
NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ ...
 1-70 1.57e-08

NH3-dependent NAD+ synthetase [Coenzyme transport and metabolism]; NH3-dependent NAD+ synthetase is part of the Pathway/BioSystem: NAD biosynthesis


Pssm-ID: 439941 [Multi-domain]  Cd Length: 542  Bit Score: 56.39  E-value: 1.57e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17538240   1 MPRVVIGMSGGVDSAVSAFLL-----KKRgfdVIGLHMinwdvQEEGTShcPRSKDesDARNVCDRLNIPFHTVN 70
Cdd:COG0171 286 FKGVVLGLSGGIDSALVAALAvdalgPEN---VLGVTM-----PSRYTS--DESLE--DAEELAENLGIEYEEID 348
TtuA-like cd01993
tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) ...
 3-134 9.25e-08

tRNA-5-methyluridine(54) 2-sulfurtransferase and similar proteins; tRNA-5-methyluridine(54) 2-sulfurtransferase, also called tRNA thiouridine synthetase TtuA, catalyzes the ATP-dependent 2-thiolation of 5-methyluridine residue at position 54 in the T loop of tRNAs, leading to 5-methyl-2-thiouridine (m(5)s(2)U or s(2)T). TtuA belongs to the adenine nucleotide alpha hydrolase superfamily (AANH) that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group. This domain has a strongly conserved motif SGGKD at the N-terminus.


Pssm-ID: 467497 [Multi-domain]  Cd Length: 190  Bit Score: 51.56  E-value: 9.25e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240   3 RVVIGMSGGVDSAVSAFLLKKRGFDVIGLHMinwDVQEEGTShcprSKDESDARNVCDRLNIPFHTVNfVKEYWNDVFLK 82
Cdd:cd01993  10 KILVAVSGGKDSLALLAVLKKLGYNVEALYI---NLGIGEYS----EKSEEVVKKLAEKLNLPLHVVD-LKEEYGLGIPE 81

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17538240  83 FLENYKNGRTTVpdidCNqSIKFDVFHKIAREKfNADFIATGH----YATTNFGDF 134
Cdd:cd01993  82 LAKKSRRPPCSV----CG-LVKRYIMNKFAVEN-GFDVVATGHnlddEAAFLLGNI 131
TilS_N cd01992
N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine ...
 3-125 1.97e-07

N-terminal domain of tRNA(Ile)-lysidine synthase and similar proteins; tRNA(Ile)-lysidine synthase (EC 6.3.4.19), also called tRNA(Ile)-2-lysyl-cytidine synthase or tRNA(Ile)-lysidine synthetase, catalyzes the ligation of lysine onto the cytidine present at position 34 of the AUA codon-specific tRNA(Ile) that contains the anticodon CAU, in an ATP-dependent manner. Cytidine is converted to lysidine, thus changing the amino acid specificity of the tRNA from methionine to isoleucine. This subfamily belongs to the adenine nucleotide alpha hydrolase superfamily that also includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to adenosine group. This domain has a strongly conserved motif SGGXD at the N-terminus.


Pssm-ID: 467496 [Multi-domain]  Cd Length: 185  Bit Score: 50.67  E-value: 1.97e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240   3 RVVIGMSGGVDSAVSAFLLK----KRGFDVIGLHmINWDVQEEgtshcprSKDESD-ARNVCDRLNIPFHTVNFVKEYwn 77
Cdd:cd01992   1 KILVAVSGGPDSMALLHLLKelrpKLGLKLVAVH-VDHGLREE-------SAEEAQfVAKLCKKLGIPLHILTVTEAP-- 70

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 17538240  78 dvflKFLENY-KNGRTtvpdidcnqsIKFDVFHKIAREkFNADFIATGH 125
Cdd:cd01992  71 ----KSGGNLeAAARE----------ARYAFLERAAKE-HGIDVLLTAH 104
QueC-like cd01995
7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC ...
 3-90 1.25e-06

7-cyano-7-deazaguanine synthase QueC and similar proteins; 7-cyano-7-deazaguanine synthase (EC 6.3.4.20) is also called 7-cyano-7-carbaguanine synthase, preQ(0) synthase, or queuosine biosynthesis protein QueC. It catalyzes the ATP-dependent conversion of 7-carboxy-7-deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)), as part of the biosynthesis pathway of queuosine (Q). Q is one of the most complex modifications occurring at the wobble position of tRNAs with GUN anticodons, and is implicated in a number of biological activities, including accuracy of decoding, virulence, and cellular differentiation. This subfamily belongs to the adenine nucleotide alpha hydrolase (AANH) superfamily that also includes other N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467499 [Multi-domain]  Cd Length: 208  Bit Score: 48.76  E-value: 1.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240   3 RVVIGMSGGVDSAVSAFLLKKRGFDVIGLHmINWdvqeeGTSHcpRSKDESDARNVCDRLNIPFHTVN--FVKEYWNDVF 80
Cdd:cd01995   2 KAVVLLSGGLDSTTLLYWALKEGYEVHALT-FDY-----GQRH--AKEELEAAKLIAKLLGIEHKVIDlsFLGELGGSSL 73

                        90
                ....*....|
gi 17538240  81 LKFLENYKNG 90
Cdd:cd01995  74 TDEGEEVPDG 83
PPase_ThiI cd01712
pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole ...
 3-124 1.28e-06

pyrophosphatase domain of thiamine biosynthesis protein ThiI; ThiI is required for thiazole synthesis in the thiamine biosynthesis pathway. ThiI is also responsible for the 4-thiouridine (S4U) modification at position 8 in some prokaryotic tRNAs. ThiI contains a PP-loop pyrophosphatase domain which binds ATP and activates tRNA by adenylation. The PP-loop pyrophosphatase catalytic domain of ThiI proteins is always accompanied by a THUMP domain towards the N terminus. THUMP domains are predicted to bind RNA and are widespread in bacteria, archaea, and eukaryotes. The acronym was derived from the names of RNA-modifying enzymes in which this domain is found, namely, thiouridine synthases (ThiI), methylases, and archaeal pseudouridine synthases. ThiI proteins from gamma-proteobacteria and from archaea of the genus Thermoplasma also contain a C-terminal extension of approximately 100 amino acid residues which accepts sulfur in the form of a persulfide on a cysteine residue. This persulfide is responsible for a nucleophilic attack of the adenylated tRNA substrate, completing the sulfur insertion forming a disulfide-bridge between the rhodanese-like domain and a second cysteine residue located in the PP-loop domain. The reaction releases AMP and modified tRNA, and leaves the enzyme in an oxidized state. The disulfide is then reductively cleaved to complete the enzymatic cycle. The pyrophosphatase domain of ThiI belongs to the adenine nucleotide hydrolase (AANH) superfamily and it binds to adenosine nucleotide.


Pssm-ID: 467485 [Multi-domain]  Cd Length: 185  Bit Score: 48.32  E-value: 1.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240   3 RVVIGMSGGVDSAVSAFLLKKRGFDVIGLHMINwdvqeeGTSHCPRSKDEsdARNVCDRL-----NIPFHTVNFVKEYWN 77
Cdd:cd01712   6 KVLVLLSGGIDSPVAAWMMMKRGVEVDFLHFHS------GPYTSEKAVEK--VKDLARVLseyqgGVKLYLVPFTDKIQK 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 17538240  78 DVFLKFLENYkngRTTVpdidcnqsIKFdVFHKIAR---EKFNADFIATG 124
Cdd:cd01712  78 EILEKVPESY---RIVL--------MRR-MMYRIAEkiaERLGADALVTG 115
NAD_synthase cd00553
NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de ...
 3-70 2.48e-06

NAD(+) synthase; NAD(+) synthase (EC 6.3.5.1), a homodimer, catalyzes the final step in the de novo nicotinamide adenine dinucleotide (NAD(+)) biosynthesis, an amide transfer from either ammonia or glutamine to nicotinic acid adenine dinucleotide (NaAD). The conversion of NaAD to NAD(+) occurs via a NAD-adenylate intermediate and requires ATP and Mg(2+). The intermediate is subsequently cleaved into NAD(+) and AMP. In many prokaryotes, such as Escherichia coli, NAD synthase consists of a single domain and is strictly ammonia dependent. In contrast, eukaryotes and other prokaryotes have an additional N-terminal amidohydrolase domain that prefer glutamine. Interestingly, NAD(+) synthases in these prokaryotes, can also utilize ammonia as an amide source.


Pssm-ID: 467484 [Multi-domain]  Cd Length: 248  Bit Score: 48.32  E-value: 2.48e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240   3 RVVIGMSGGVDSAVSAFLLKK--RGFDVIGLHMINWDVQEEgtshcprskDESDARNVCDRLNIPFHTVN 70
Cdd:cd00553  25 GFVLGLSGGIDSAVVAALAVRalGAENVLALIMPSRYSSKE---------TRDDAKALAENLGIEYRTID 85
NAD_synthase pfam02540
NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is ...
 4-236 2.94e-06

NAD synthase; NAD synthase (EC:6.3.5.1) is involved in the de novo synthesis of NAD and is induced by stress factors such as heat shock and glucose limitation.


Pssm-ID: 396888 [Multi-domain]  Cd Length: 241  Bit Score: 48.15  E-value: 2.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240     4 VVIGMSGGVDSAVSAFLLKKRGFD--VIGLHMINWDVQEEgtshcprskDESDARNVCDRLNIPFHTVNFvkeywNDVFL 81
Cdd:pfam02540  21 VVLGLSGGIDSSLVAYLAVKALGKenVLALIMPSSQSSEE---------DVQDALALAENLGIEYKTIDI-----KPIVR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240    82 KFLENYKNGRTTVPDIDCNQSIKFDVFHKIArEKFNADFIATGHYA------TTNFGDfqqnakdsdeirlfsgkdplkd 155
Cdd:pfam02540  87 AFSQLFQDASEDFAKGNLKARIRMAILYYIA-NKFNYLVLGTGNKSelavgyFTKYGD---------------------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240   156 qtfflctvnqeqLKRAMFPLGSLQKSEVKRIAEEQGF-QEVAKKP------------ESMGICFigkkkrfsDFLDEYIE 222
Cdd:pfam02540 144 ------------GACDIAPIGDLYKTQVYELARYLNVpERIIKKPpsadlwpgqtdeEELGIPY--------DELDDILK 203

                         250
                  ....*....|....*....
gi 17538240   223 -----PKPGRILLKNGSEI 236
Cdd:pfam02540 204 lvekkLSPEEIIGKGLPAE 222
PRK08349 PRK08349
hypothetical protein; Validated
 3-200 1.49e-05

hypothetical protein; Validated


Pssm-ID: 169396  Cd Length: 198  Bit Score: 45.50  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240    3 RVVIGMSGGVDSAVSAFLLKKRGFDVIGLHMINWDVQEEGTSHCPRSKDESDARNVCDrlnipFHTVNFVkEYWNDVFLK 82
Cdd:PRK08349   2 KAVALLSSGIDSPVAIYLMLRRGVEVYPVHFRQDEKKEEKVRELVERLQELHGGKLKD-----PVVVDAF-EEQGPVFEK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240   83 FLENyKNGRTTVpdIDCNQSIkFDVFHKIAREKfNADFIATGHyattNFGDFQQNAKDSdeirlfsgkdplkdqtffLCT 162
Cdd:PRK08349  76 LREL-KKEKWTC--IFCKYTM-YRKAERIAHEI-GASAIITGD----SLGQVASQTLDN------------------LMV 128

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 17538240  163 VNQEQLKRAMFPLGSLQKSEVKRIAEEQGFQEVAKKPE 200
Cdd:PRK08349 129 ISTATDLPVLRPLIGLDKEEIVKIAKEIGTFEISIEPE 166
ATP_bind_3 pfam01171
PP-loop family; This family of proteins belongs to the PP-loop superfamily.
 6-191 1.65e-05

PP-loop family; This family of proteins belongs to the PP-loop superfamily.


Pssm-ID: 426097 [Multi-domain]  Cd Length: 178  Bit Score: 44.93  E-value: 1.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240     6 IGMSGGVDSAVSAFLLKK----RGFDVIGLHmINWDVQEEgtshcprSKDESD-ARNVCDRLNIPFHTVNFvkeywnDVF 80
Cdd:pfam01171   1 VAVSGGPDSMALLYLLAKlkikLGIELTAAH-VNHGLREE-------SDREAEhVQALCRQLGIPLEILRV------DVA 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240    81 LKFLENY-KNGRTtvpdidcnqsIKFDVFHKIArEKFNADFIATGHyattNFGDFQQNAKdsdeIRLFSGKDPL-----K 154
Cdd:pfam01171  67 KKSGENLeAAARE----------ARYDFFEEAL-KKHGADVLLTAH----HLDDQLETFL----MRLKRGSGLAglagiP 127

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 17538240   155 DQTFFLCtvnqEQLKRamfPLGSLQKSEVKRIAEEQG 191
Cdd:pfam01171 128 PVREFAG----GRIIR---PLLKVSKAEIEAYAKEHK 157
QueC COG0603
7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and ...
 1-75 5.38e-05

7-cyano-7-deazaguanine synthase (queuosine biosynthesis) [Translation, ribosomal structure and biogenesis]; 7-cyano-7-deazaguanine synthase (queuosine biosynthesis) is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440368 [Multi-domain]  Cd Length: 223  Bit Score: 44.00  E-value: 5.38e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17538240   1 MPRVVIGMSGGVDSAVSAFLLKKRGFDVIGLHmINwdvqeEGtshcPRSKDESD-ARNVCDRLNIPFHTV---NFVKEY 75
Cdd:COG0603   2 MKKAVVLLSGGLDSTTCLAWALARGYEVYALS-FD-----YG----QRHRKELEaARRIAKALGVGEHKVidlDFLGEI 70
ThiI pfam02568
Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for ...
 3-35 7.96e-05

Thiamine biosynthesis protein (ThiI); ThiI is required for thiazole synthesis, required for thiamine biosynthesis.


Pssm-ID: 280691 [Multi-domain]  Cd Length: 197  Bit Score: 43.19  E-value: 7.96e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 17538240     3 RVVIGMSGGVDSAVSAFLLKKRGFDVIGLHMIN 35
Cdd:pfam02568   5 KVLALISGGIDSPVAAYMMMRRGCRVVALHFIN 37
TIGR00342 TIGR00342
tRNA sulfurtransferase ThiI; Members of this protein family are "ThiI", a sulfurtransferase ...
 3-35 1.65e-04

tRNA sulfurtransferase ThiI; Members of this protein family are "ThiI", a sulfurtransferase involved in 4-thiouridine modification of tRNA. This protein often is bifunctional, with genetically separable activities, where the C-terminal rhodanese-like domain (residues 385 to 482 in E. coli ThiI), a domain not included in this model, is sufficient to synthesize the thiazole moiety of thiamine (see TIGR04271). Note that ThiI, because of its role in tRNA modification, may occur in species (such as Mycoplasma genitalium) that lack de novo thiamine biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine, Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273025 [Multi-domain]  Cd Length: 371  Bit Score: 43.17  E-value: 1.65e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 17538240     3 RVVIGMSGGVDSAVSAFLLKKRGFDVIGLHMIN 35
Cdd:TIGR00342 174 KVLALLSGGIDSPVAAFMMMKRGCRVVAVHFFN 206
CTU1-like cd01713
cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human ...
 3-145 6.25e-04

cytoplasmic tRNA 2-thiolation protein 1 and similar proteins; This subfamily includes human cytoplasmic tRNA 2-thiolation protein 1, also called cytosolic thiouridylase subunit 1 (CTU1), ATP-binding domain-containing protein 3 (ATPBD3), cancer-associated gene protein, or cytoplasmic tRNA adenylyltransferase 1. CTU1 plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). It directly binds tRNAs and probably acts by catalyzing adenylation of tRNAs, an intermediate required for 2-thiolation. The CTU1-like subfamily belongs to the nucleotide alpha hydrolase (AANH) superfamily that includes N-type ATP PPases and ATP sulfurylases. It forms an alpha/beta/alpha fold which binds to the adenosine group.


Pssm-ID: 467486  Cd Length: 208  Bit Score: 40.65  E-value: 6.25e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240   3 RVVIGMSGGVDSAVSAFLLK---KRGFDVIGLHMINWDvqeEGTSHCpRSKDESDARNVCDRLNIPFHTVNFVKEYwnDV 79
Cdd:cd01713  20 RVAVGLSGGKDSTVLLYVLKelnKRHDYGVELIAVTID---EGIKGY-RDDSLEAARKLAEEYGIPLEIVSFEDEF--GF 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240  80 FLKFLENYKNGRTTvpdiDCNqsikFD-VF-----HKIAREkFNADFIATGH----YATT---NF--GDFQQNAKDSDEI 144
Cdd:cd01713  94 TLDELIVGKGGKKN----ACT----YCgVFrrralNRGARE-LGADKLATGHnlddEAETilmNLlrGDVARLLRTGPEP 164


                .
gi 17538240 145 R 145
Cdd:cd01713 165 R 165
nadE TIGR00552
NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the ...
 4-69 7.22e-04

NAD+ synthetase; NAD+ synthetase is a nearly ubiquitous enzyme for the final step in the biosynthesis of the essensial cofactor NAD. The member of this family from Bacillus subtilis is a strictly NH(3)-dependent NAD(+) synthetase of 272 amino acids. Proteins consisting only of the domain modeled here may be named as NH3-dependent NAD+ synthetase. Amidotransferase activity may reside in a separate protein, or not be present. Some other members of the family, such as from Mycobacterium tuberculosis, are considerably longer, contain an apparent amidotransferase domain, and show glutamine-dependent as well as NH(3)-dependent activity. [Biosynthesis of cofactors, prosthetic groups, and carriers, Pyridine nucleotides]


Pssm-ID: 273132 [Multi-domain]  Cd Length: 250  Bit Score: 40.83  E-value: 7.22e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17538240     4 VVIGMSGGVDSAVSAFLLKKR-GFDVIGLHMINWDVQEEgtshcprsKDESDARNVCDRLNIPFHTV 69
Cdd:TIGR00552  25 VVLGLSGGIDSAVVAALCVEAlGEQNHALLLPHSVQTPE--------QDVQDALALAEPLGINYKNI 83
ThiI COG0301
Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme ...
 3-124 8.77e-04

Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) [Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis]; Adenylyl- and sulfurtransferase ThiI (thiamine and tRNA 4-thiouridine biosynthesis) is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440070 [Multi-domain]  Cd Length: 382  Bit Score: 40.84  E-value: 8.77e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240   3 RVVIGMSGGVDSAVSAFLLKKRGFDVIGLHMINwdvqeeGTSHCPRSKDesDARNVCDRLN------IPFHTVNFVkeyw 76
Cdd:COG0301 176 KVLLLLSGGIDSPVAAYLMMKRGVEVEAVHFHS------GPYTSERAEE--KVKDLARKLSrygghrVKLYVVPFT---- 243

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 17538240  77 nDVFLKFLENYKNGRTTVpdidcnqsikfdVF----HKIA---REKFNADFIATG 124
Cdd:COG0301 244 -EVQEEILEKVPERYRTV------------LLrrmmMRIAeriAEKEGALALVTG 285
QueC pfam06508
Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis ...
 3-70 9.07e-04

Queuosine biosynthesis protein QueC; This family of proteins participate in the biosynthesis of 7-carboxy-7-deazaguanine. They catalyze the conversion of 7-deaza-7-carboxyguanine to preQ0.


Pssm-ID: 428982 [Multi-domain]  Cd Length: 210  Bit Score: 40.29  E-value: 9.07e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17538240     3 RVVIGMSGGVDSAVSAFLLKKRGFDVIGLHMiNWdvqeeGTSHcprSKDESDARNVCDRLNIPFHTVN 70
Cdd:pfam06508   1 KAVVLLSGGLDSTTCLAWAKKEGYEVYALSF-DY-----GQRH---RKELECAKKIAKALGVEHKILD 59
guaA PRK00074
GMP synthase; Reviewed
 3-23 1.09e-03

GMP synthase; Reviewed


Pssm-ID: 234614 [Multi-domain]  Cd Length: 511  Bit Score: 40.80  E-value: 1.09e-03
                         10        20
                 ....*....|....*....|.
gi 17538240    3 RVVIGMSGGVDSAVSAFLLKK 23
Cdd:PRK00074 217 KVILGLSGGVDSSVAAVLLHK 237
COG1365 COG1365
Predicted ATPase, PP-loop superfamily [General function prediction only];
2-93 3.15e-03

Predicted ATPase, PP-loop superfamily [General function prediction only];


Pssm-ID: 440976  Cd Length: 256  Bit Score: 38.88  E-value: 3.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17538240   2 PRVVIGMSGGVDSAVSAFLLKKRGFDVIGlhminwdVQEEGTSHCPRSKDESdARNVCDRLNIPfHTvnFVKEYWNDVFl 81
Cdd:COG1365  61 PKVVVAFSGGVDSSASLIIAKWIGFDVEA-------VTVKSTIILPQMFKKN-IKELCKKLNVK-HE--FIEIDLGEII- 128

                        90
                ....*....|..
gi 17538240  82 kflENYKNGRTT 93
Cdd:COG1365 129 ---EDALKGKFH 137
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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